Calbindin 1

CALB1
Identifiers
Aliases	CALB1, CALB, D-28K, calbindin 1
External IDs	OMIM: 114050 MGI: 88248 HomoloGene: 21026 GeneCards: CALB1
Gene location (Human) Chr. Chromosome 8 (human) Band 8q21.3 Start 90,058,608 bp End 90,095,475 bp
Gene location (Mouse) Chr. Chromosome 4 (mouse) Band 4 A2|4 6.66 cM Start 15,881,264 bp End 15,908,064 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in kidney tubule cerebellar vermis kidney nucleus accumbens glomerulus metanephric glomerulus caudate nucleus renal medulla putamen orbitofrontal cortex Top expressed in molar cerebellar vermis ventromedial nucleus mammillary body medial dorsal nucleus paraventricular nucleus of hypothalamus medial geniculate nucleus arcuate nucleus globus pallidus nucleus accumbens More reference expression data BioGPS n/a
Gene ontology Molecular function calcium ion binding zinc ion binding metal ion binding protein binding vitamin D binding calcium ion binding involved in regulation of presynaptic cytosolic calcium ion concentration calcium ion binding involved in regulation of postsynaptic cytosolic calcium ion concentration Cellular component cytoplasm cell body synapse intracellular anatomical structure axon terminal bouton neuronal cell body dendrite neuron projection extracellular exosome nucleus cytosol dendritic spine calyx of Held hippocampal mossy fiber to CA3 synapse postsynapse glutamatergic synapse GABA-ergic synapse presynaptic cytosol postsynaptic cytosol stereocilium cuticular plate Biological process cellular response to organic substance retina layer formation regulation of cytosolic calcium ion concentration calcium ion homeostasis locomotory behavior metanephric distal convoluted tubule development regulation of synaptic plasticity metanephric part of ureteric bud development long-term memory metanephric connecting tubule development retina development in camera-type eye short-term memory learning or memory metanephric collecting duct development regulation of presynaptic cytosolic calcium ion concentration regulation of long-term synaptic potentiation regulation of postsynaptic cytosolic calcium ion concentration cochlea development Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 793 12307 Ensembl ENSG00000104327 ENSMUSG00000028222 UniProt P05937 P12658 RefSeq (mRNA) NM_004929 NM_001366795 NM_009788 RefSeq (protein) NP_004920 NP_001353724 NP_033918 Location (UCSC) Chr 8: 90.06 – 90.1 Mb Chr 4: 15.88 – 15.91 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Calbindin 1 is a protein that in humans is encoded by the CALB1 gene. It belongs to the calbindin family of calcium-binding proteins, along with calretinin (CALB2).

Function

The protein encoded by this gene is a member of the calcium-binding protein superfamily that includes calmodulin and troponin C. Originally described as a 27 kDa protein, it is now known to be a 28 kDa protein. It contains four active calcium-binding domains, and has two modified domains that are thought to have lost their calcium binding capability. This protein is thought to buffer entry of calcium upon stimulation of glutamate receptors. Depletion of this protein was noted in patients with Huntington disease. [provided by RefSeq, Jan 2015].

Further reading

• Tao L, Murphy ME, English AM (May 2002). "S-nitrosation of Ca(2+)-loaded and Ca(2+)-free recombinant calbindin D(28K) from human brain". Biochemistry. 41 (19): 6185–92. doi:10.1021/bi015846+. PMID 11994015.
• Berggard T, Szczepankiewicz O, Thulin E, Linse S (November 2002). "Myo-inositol monophosphatase is an activated target of calbindin D28k". J. Biol. Chem. 277 (44): 41954–9. doi:10.1074/jbc.M203492200. PMID 12176979.
• Belkacemi L, Gariépy G, Mounier C, Simoneau L, Lafond J (June 2003). "Expression of calbindin-D28k (CaBP28k) in trophoblasts from human term placenta". Biol. Reprod. 68 (6): 1943–50. doi:10.1095/biolreprod.102.009373. PMID 12606474.
• Cedervall T, Berggård T, Borek V, Thulin E, Linse S, Akerfeldt KS (January 2005). "Redox sensitive cysteine residues in calbindin D28k are structurally and functionally important". Biochemistry. 44 (2): 684–93. doi:10.1021/bi049232r. PMID 15641794.
• Vanbelle C, Halgand F, Cedervall T, Thulin E, Akerfeldt KS, Laprévote O, Linse S (April 2005). "Deamidation and disulfide bridge formation in human calbindin D28k with effects on calcium binding". Protein Sci. 14 (4): 968–79. doi:10.1110/ps.041157705. PMC 2253450. PMID 15741335.
• Valencia I, Legido A, Yelin K, Khurana D, Kothare SV, Katsetos CD (December 2006). "Anomalous inhibitory circuits in cortical tubers of human tuberous sclerosis complex associated with refractory epilepsy: aberrant expression of parvalbumin and calbindin-D28k in dysplastic cortex". J. Child Neurol. 21 (12): 1058–63. doi:10.1177/7010.2006.00242. PMID 17156698. S2CID 36971471.
• Vig PJ, Wei J, Shao Q, Hebert MD, Subramony SH, Sutton LT (June 2007). "Role of tissue transglutaminase type 2 in calbindin-D28k interaction with ataxin-1". Neurosci. Lett. 420 (1): 53–7. doi:10.1016/j.neulet.2007.04.005. PMC 1949022. PMID 17442486.
• Zhang C, Sun Y, Wang W, Zhang Y, Ma M, Lou Z (February 2008). "Crystallization and preliminary crystallographic analysis of human Ca 2+-loaded calbindin-D28k". Acta Crystallographica Section F. 64 (Pt 2): 133–6. doi:10.1107/S1744309108001905. PMC 2374171. PMID 18259068.
• Bauer MC, Nilsson H, Thulin E, Frohm B, Malm J, Linse S (April 2008). "Zn2+ binding to human calbindin D(28k) and the role of histidine residues". Protein Sci. 17 (4): 760–7. doi:10.1110/ps.073381108. PMC 2271158. PMID 18359862.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.